The amino-terminal signal peptide on the porcine transmissible gastroenteritis coronavirus matrix protein is not an absolute requirement for membrane translocation and glycosylation.
Identifieur interne : 001C57 ( Main/Exploration ); précédent : 001C56; suivant : 001C58The amino-terminal signal peptide on the porcine transmissible gastroenteritis coronavirus matrix protein is not an absolute requirement for membrane translocation and glycosylation.
Auteurs : P A Kapke [États-Unis] ; F Y Tung ; B G Hogue ; D A Brian ; R D Woods ; R. WesleySource :
- Virology [ 0042-6822 ] ; 1988.
Descripteurs français
- KwdFr :
- Biosynthèse des protéines, Clonage moléculaire, Coronaviridae (physiologie), Données de séquences moléculaires, Glycosylation, Maturation post-traductionnelle des protéines, Membrane cellulaire (métabolisme), Protéines de la matrice virale (génétique), Protéines de la matrice virale (physiologie), Relation structure-activité, Signaux de triage des protéines (physiologie), Séquence d'acides aminés, Séquence nucléotidique, Transport biologique, Virus de la gastroentérite transmissible (physiologie).
- MESH :
- génétique : Protéines de la matrice virale.
- métabolisme : Membrane cellulaire.
- physiologie : Coronaviridae, Protéines de la matrice virale, Signaux de triage des protéines, Virus de la gastroentérite transmissible.
- Biosynthèse des protéines, Clonage moléculaire, Données de séquences moléculaires, Glycosylation, Maturation post-traductionnelle des protéines, Relation structure-activité, Séquence d'acides aminés, Séquence nucléotidique, Transport biologique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Base Sequence, Biological Transport, Cell Membrane (metabolism), Cloning, Molecular, Coronaviridae (physiology), Glycosylation, Molecular Sequence Data, Protein Biosynthesis, Protein Processing, Post-Translational, Protein Sorting Signals (physiology), Structure-Activity Relationship, Transmissible gastroenteritis virus (physiology), Viral Matrix Proteins (genetics), Viral Matrix Proteins (physiology).
- MESH :
- chemical , genetics : Viral Matrix Proteins.
- chemical , physiology : Protein Sorting Signals, Viral Matrix Proteins.
- metabolism : Cell Membrane.
- physiology : Coronaviridae, Transmissible gastroenteritis virus.
- Amino Acid Sequence, Base Sequence, Biological Transport, Cloning, Molecular, Glycosylation, Molecular Sequence Data, Protein Biosynthesis, Protein Processing, Post-Translational, Structure-Activity Relationship.
Abstract
cDNA clones mapping within the first 2601 bases of the 3' end of the porcine transmissible gastroenteritis corona-virus (TGEV) genome were sequenced by the method of Maxam and Gilbert and an open reading frame yielding a protein having properties of the matrix (M or E1) protein was identified. It is positioned at the 5' side of the nucleocapsid (N) gene from which it is separated by an intergenic stretch of 12 bases. The deduced M protein comprises 262 amino acids, has a molecular weight of 29,544, is moderately hydrophobic, and has a net charge of +7 at neutral pH. Thirty-four percent of its amino acid sequence is homologous with the M protein of the bovine coronavirus (BCV), 32% with that of the mouse hepatitis coronavirus (MHV), and 19% with that of the avian infectious bronchitis coronavirus (IBV). Judging from alignment with the BCV, MHV, and IBV M proteins, the amino terminus of the TGEV M protein extends 54 amino acids from the virion envelope which compares with only 28 for BCV, 26 for MHV, and 21 for IBV. Eleven of the sixteen amino-terminal amino acids are hydrophobic and the positions of charged amino acids around this sequence suggest that the first 16 amino acids comprise a potentially cleavable signal peptide for membrane insertion. A similar sequence is not found in the M proteins of BCV, MHV, or IBV. When mRNA from infected cells, or RNA prepared by in vitro transcription of the reconstructed M gene, was translated in vitro in the presence of microsomes, the M protein became translocated and glycosylated. When a protein without the amino-terminal signal peptide was made by translating a truncated version of the M gene transcript, some translocation and glycosylation also occurred suggesting that the amino-terminal signal peptide on the TGEV M protein is not an absolute requirement for membrane translocation. Interestingly, the amino-terminal peptide did not appear to be cleaved during in vitro translation in the presence of microsomes suggesting that a step in virion assembly may be required for proper exposure of the cleavage site to the signal peptidase.
DOI: 10.1016/0042-6822(88)90581-8
PubMed: 2841792
Affiliations:
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Le document en format XML
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<term>Base Sequence</term>
<term>Biological Transport</term>
<term>Cell Membrane (metabolism)</term>
<term>Cloning, Molecular</term>
<term>Coronaviridae (physiology)</term>
<term>Glycosylation</term>
<term>Molecular Sequence Data</term>
<term>Protein Biosynthesis</term>
<term>Protein Processing, Post-Translational</term>
<term>Protein Sorting Signals (physiology)</term>
<term>Structure-Activity Relationship</term>
<term>Transmissible gastroenteritis virus (physiology)</term>
<term>Viral Matrix Proteins (genetics)</term>
<term>Viral Matrix Proteins (physiology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Biosynthèse des protéines</term>
<term>Clonage moléculaire</term>
<term>Coronaviridae (physiologie)</term>
<term>Données de séquences moléculaires</term>
<term>Glycosylation</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Protéines de la matrice virale (génétique)</term>
<term>Protéines de la matrice virale (physiologie)</term>
<term>Relation structure-activité</term>
<term>Signaux de triage des protéines (physiologie)</term>
<term>Séquence d'acides aminés</term>
<term>Séquence nucléotidique</term>
<term>Transport biologique</term>
<term>Virus de la gastroentérite transmissible (physiologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Viral Matrix Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Protein Sorting Signals</term>
<term>Viral Matrix Proteins</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de la matrice virale</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Membrane cellulaire</term>
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<term>Protéines de la matrice virale</term>
<term>Signaux de triage des protéines</term>
<term>Virus de la gastroentérite transmissible</term>
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<term>Transmissible gastroenteritis virus</term>
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<term>Base Sequence</term>
<term>Biological Transport</term>
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<term>Glycosylation</term>
<term>Molecular Sequence Data</term>
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<term>Structure-Activity Relationship</term>
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<term>Données de séquences moléculaires</term>
<term>Glycosylation</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Relation structure-activité</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">cDNA clones mapping within the first 2601 bases of the 3' end of the porcine transmissible gastroenteritis corona-virus (TGEV) genome were sequenced by the method of Maxam and Gilbert and an open reading frame yielding a protein having properties of the matrix (M or E1) protein was identified. It is positioned at the 5' side of the nucleocapsid (N) gene from which it is separated by an intergenic stretch of 12 bases. The deduced M protein comprises 262 amino acids, has a molecular weight of 29,544, is moderately hydrophobic, and has a net charge of +7 at neutral pH. Thirty-four percent of its amino acid sequence is homologous with the M protein of the bovine coronavirus (BCV), 32% with that of the mouse hepatitis coronavirus (MHV), and 19% with that of the avian infectious bronchitis coronavirus (IBV). Judging from alignment with the BCV, MHV, and IBV M proteins, the amino terminus of the TGEV M protein extends 54 amino acids from the virion envelope which compares with only 28 for BCV, 26 for MHV, and 21 for IBV. Eleven of the sixteen amino-terminal amino acids are hydrophobic and the positions of charged amino acids around this sequence suggest that the first 16 amino acids comprise a potentially cleavable signal peptide for membrane insertion. A similar sequence is not found in the M proteins of BCV, MHV, or IBV. When mRNA from infected cells, or RNA prepared by in vitro transcription of the reconstructed M gene, was translated in vitro in the presence of microsomes, the M protein became translocated and glycosylated. When a protein without the amino-terminal signal peptide was made by translating a truncated version of the M gene transcript, some translocation and glycosylation also occurred suggesting that the amino-terminal signal peptide on the TGEV M protein is not an absolute requirement for membrane translocation. Interestingly, the amino-terminal peptide did not appear to be cleaved during in vitro translation in the presence of microsomes suggesting that a step in virion assembly may be required for proper exposure of the cleavage site to the signal peptidase.</div>
</front>
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